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CAZyme Information: MGYG000000345_02315

You are here: Home > Sequence: MGYG000000345_02315

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species UBA1829 sp002338895
Lineage Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; UBA1829; UBA1829; UBA1829 sp002338895
CAZyme ID MGYG000000345_02315
CAZy Family GT2
CAZyme Description Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
461 MGYG000000345_15|CGC2 51481.4 8.8764
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000345 3773289 MAG Sweden Europe
Gene Location Start: 58239;  End: 59624  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000345_02315.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT2 85 252 3.8e-34 0.9705882352941176

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06434 GT2_HAS 1.09e-50 84 321 2 235
Hyaluronan synthases catalyze polymerization of hyaluronan. Hyaluronan synthases (HASs) are bi-functional glycosyltransferases that catalyze polymerization of hyaluronan. HASs transfer both GlcUA and GlcNAc in beta-(1,3) and beta-(1,4) linkages, respectively to the hyaluronan chain using UDP-GlcNAc and UDP-GlcUA as substrates. HA is made as a free glycan, not attached to a protein or lipid. HASs do not need a primer for HA synthesis; they initiate HA biosynthesis de novo with only UDP-GlcNAc, UDP-GlcUA, and Mg2+. Hyaluronan (HA) is a linear heteropolysaccharide composed of (1-3)-linked beta-D-GlcUA-beta-D-GlcNAc disaccharide repeats. It can be found in vertebrates and a few microbes and is typically on the cell surface or in the extracellular space, but is also found inside mammalian cells. Hyaluronan has several physiochemical and biological functions such as space filling, lubrication, and providing a hydrated matrix through which cells can migrate.
cd06423 CESA_like 7.75e-47 86 274 1 180
CESA_like is the cellulose synthase superfamily. The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of Glucan.
COG1215 BcsA 1.08e-45 40 436 10 422
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility].
cd06439 CESA_like_1 7.85e-43 57 305 3 235
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily. This is a subfamily of cellulose synthase (CESA) superfamily. CESA superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members of the superfamily include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins.
pfam00535 Glycos_transf_2 2.83e-32 85 252 1 164
Glycosyl transferase family 2. Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CBX26966.1 6.13e-122 39 447 58 465
ACN15324.1 1.22e-117 63 436 71 443
BCS52180.1 1.34e-117 45 436 49 439
ACN17701.1 1.16e-112 63 443 64 443
QBH12450.1 1.28e-112 63 437 68 441

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6YV7_B 9.61e-15 64 279 16 226
MannosyltransferasePcManGT from Pyrobaculum calidifontis [Pyrobaculum calidifontis JCM 11548],6YV8_B Mannosyltransferase PcManGT from Pyrobaculum calidifontis in complex with GDP and Mn2+ [Pyrobaculum calidifontis JCM 11548],6YV9_A Mannosyltransferase PcManGT from Pyrobaculum calidifontis in complex with GDP-Man and Mn2+ [Pyrobaculum calidifontis JCM 11548]
6YV7_A 9.68e-15 64 279 17 227
MannosyltransferasePcManGT from Pyrobaculum calidifontis [Pyrobaculum calidifontis JCM 11548],6YV8_A Mannosyltransferase PcManGT from Pyrobaculum calidifontis in complex with GDP and Mn2+ [Pyrobaculum calidifontis JCM 11548],6YV9_B Mannosyltransferase PcManGT from Pyrobaculum calidifontis in complex with GDP-Man and Mn2+ [Pyrobaculum calidifontis JCM 11548]
6P61_A 4.80e-10 79 245 10 173
Structureof a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197],6P61_B Structure of a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197],6P61_C Structure of a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197],6P61_D Structure of a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197]
5TZE_C 4.54e-08 83 188 2 106
Crystalstructure of S. aureus TarS in complex with UDP-GlcNAc [Staphylococcus aureus],5TZE_E Crystal structure of S. aureus TarS in complex with UDP-GlcNAc [Staphylococcus aureus],5TZI_C Crystal structure of S. aureus TarS 1-349 [Staphylococcus aureus],5TZJ_A Crystal structure of S. aureus TarS 1-349 in complex with UDP-GlcNAc [Staphylococcus aureus],5TZJ_C Crystal structure of S. aureus TarS 1-349 in complex with UDP-GlcNAc [Staphylococcus aureus],5TZK_C Crystal structure of S. aureus TarS 1-349 in complex with UDP [Staphylococcus aureus]
5TZ8_A 6.61e-08 83 188 2 106
Crystalstructure of S. aureus TarS [Staphylococcus aureus],5TZ8_B Crystal structure of S. aureus TarS [Staphylococcus aureus],5TZ8_C Crystal structure of S. aureus TarS [Staphylococcus aureus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P04340 3.43e-41 76 437 43 395
N-acetylglucosaminyltransferase OS=Rhizobium leguminosarum bv. viciae OX=387 GN=nodC PE=3 SV=1
Q07755 1.43e-40 76 436 39 394
N-acetylglucosaminyltransferase OS=Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 / NCIMB 13405 / ORS 571) OX=438753 GN=nodC PE=3 SV=2
P72334 1.47e-40 62 438 25 397
N-acetylglucosaminyltransferase OS=Rhizobium sp. (strain N33) OX=103798 GN=nodC PE=3 SV=1
P04341 6.70e-40 76 363 43 330
N-acetylglucosaminyltransferase OS=Rhizobium meliloti (strain 1021) OX=266834 GN=nodC PE=3 SV=1
P17862 3.29e-39 82 437 49 396
N-acetylglucosaminyltransferase OS=Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099) OX=266835 GN=nodC PE=3 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000026 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      download full data without filtering help

start end
15 37
44 66
347 369
374 396
406 428